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Volumn 138, Issue 1, 2004, Pages 67-74

A new method to purify hepatic CYP1A of Prochilodus scrofa, a Brazilian freshwater fish

Author keywords

Curimbat ; CYP; CYP1A; EROD; Fish; HPLC; NADPH cytochrome P450 reductase; Purification

Indexed keywords

CYTOCHROME P450 1A; ENZYME ANTIBODY; ETHOXYRESORUFIN DEETHYLASE; LIPID; PENTOXYRESORUFIN DEALKYLASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 4143070386     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2004.05.004     Document Type: Article
Times cited : (8)

References (38)
  • 1
    • 0032547713 scopus 로고    scopus 로고
    • Gel electrophoresis for studying biological function
    • Bárány M., Bárány K., Giometti C.S. Gel electrophoresis for studying biological function. Anal. Chim. Acta. 372:1998;33-66
    • (1998) Anal. Chim. Acta , vol.372 , pp. 33-66
    • Bárány, M.1    Bárány, K.2    Giometti, C.S.3
  • 2
    • 0028794689 scopus 로고
    • Cytochrome P450: Structure, function, and generation of reactive oxygen species
    • Bernhardt R. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol., Biochem. Pharmacol. 127:1995;137-221
    • (1995) Rev. Physiol., Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 3
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beier H., Gross H.J. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis. 8:1987;93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 5
    • 0031770433 scopus 로고    scopus 로고
    • Rainbow trout cytochrome P450s: Purification, molecular aspects, metabolic activity, induction and role in environmental monitoring
    • Buhler D.R., Wang-Buhler J.L. Rainbow trout cytochrome P450s: purification, molecular aspects, metabolic activity, induction and role in environmental monitoring. Comp. Biochem. Physiol. C121:1998;107-137
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 107-137
    • Buhler, D.R.1    Wang-Buhler, J.L.2
  • 6
    • 0017324522 scopus 로고
    • Enzyme topology of intracellular membranes
    • De Pierre J.W., Ernster L. Enzyme topology of intracellular membranes. Ann. Rev. Biochem. 46:1977;201-262
    • (1977) Ann. Rev. Biochem. , vol.46 , pp. 201-262
    • De Pierre, J.W.1    Ernster, L.2
  • 7
    • 0029170651 scopus 로고
    • Effects of the thermal stress on respiratory responses to hypoxia of a South American Prochilodontide fish, Prochilodus scrofa
    • Fernandes M.N., Barrionuevo W.R., Rantin F.T. Effects of the thermal stress on respiratory responses to hypoxia of a South American Prochilodontide fish, Prochilodus scrofa. J. Fish Biol. 46:1995;123-133
    • (1995) J. Fish Biol. , vol.46 , pp. 123-133
    • Fernandes, M.N.1    Barrionuevo, W.R.2    Rantin, F.T.3
  • 8
    • 0021965297 scopus 로고
    • Simultaneous purification of multiples forms of rat liver microsomal cytochrome P-450 by high-performance liquid chromatography
    • Funae Y., Imaoka S. Simultaneous purification of multiples forms of rat liver microsomal cytochrome P-450 by high-performance liquid chromatography. Biochim. Biophys. Acta. 842:1985;119-132
    • (1985) Biochim. Biophys. Acta , vol.842 , pp. 119-132
    • Funae, Y.1    Imaoka, S.2
  • 9
    • 4143075496 scopus 로고
    • Peixes do Brasil-Subordem Chariciforme
    • Piracicaba, SP: Editora Franciscana
    • Godoy M.P. Peixes do Brasil-Subordem Chariciforme. 1st ed.:1975;Editora Franciscana, Piracicaba, SP
    • (1975) 1st Ed.
    • Godoy, M.P.1
  • 10
    • 0017409770 scopus 로고
    • Separation and purification of multiple forms of microsomal cytochrome P450. Activities of different forms of cytochrome P450 towards several compounds of environmental interest
    • Guengerich F.P. Separation and purification of multiple forms of microsomal cytochrome P450. Activities of different forms of cytochrome P450 towards several compounds of environmental interest. J. Biol. Chem. 252:1977;3970-3979
    • (1977) J. Biol. Chem. , vol.252 , pp. 3970-3979
    • Guengerich, F.P.1
  • 13
    • 0032524690 scopus 로고    scopus 로고
    • Oxidation of nonionic detergents by cytochrome P450 enzymes
    • Hosea N.A., Guengerich F.P. Oxidation of nonionic detergents by cytochrome P450 enzymes. Arch. Biochem. Biophys. 353:1998;365-373
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 365-373
    • Hosea, N.A.1    Guengerich, F.P.2
  • 14
    • 0026654417 scopus 로고
    • Role of phospholipids in reconstituted cytochrome P4503A form and mechanism of their activation of catalytic activity
    • Imaoka S., Imai Y., Shimada T., Funae Y. Role of phospholipids in reconstituted cytochrome P4503A form and mechanism of their activation of catalytic activity. Biochemistry. 31:1992;6063-6069
    • (1992) Biochemistry , vol.31 , pp. 6063-6069
    • Imaoka, S.1    Imai, Y.2    Shimada, T.3    Funae, Y.4
  • 15
    • 85047697899 scopus 로고    scopus 로고
    • Epoxidation of benzo[a]pyrene-7,8-dihydrodiol by human CYP1A1 in reconstituted membranes. Effects of charge and nonbilayer phase propensity of the membrane
    • Kisselev P., Schwarz D., Platt K.L., Schunk W.H., Roots I. Epoxidation of benzo[a]pyrene-7,8-dihydrodiol by human CYP1A1 in reconstituted membranes. Effects of charge and nonbilayer phase propensity of the membrane. Eur. J. Biochem. 269:2002;1799-1805
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1799-1805
    • Kisselev, P.1    Schwarz, D.2    Platt, K.L.3    Schunk, W.H.4    Roots, I.5
  • 16
    • 0020559286 scopus 로고
    • An aryl hydrocarbon hydroxylating cytochrome P450 from the marine fish Stenotomus chrysops
    • Klotz A.V., Stegeman J.J., Walsh C. An aryl hydrocarbon hydroxylating cytochrome P450 from the marine fish Stenotomus chrysops. Arch. Biochem. Biophys. 226:1983;578-592
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 578-592
    • Klotz, A.V.1    Stegeman, J.J.2    Walsh, C.3
  • 17
    • 0019083826 scopus 로고
    • High-performance liquid chromatography technique for resolving multiples forms of hepatic membrane-bound cytochrome P450
    • Kotake A.N., Funae Y. High-performance liquid chromatography technique for resolving multiples forms of hepatic membrane-bound cytochrome P450. Proc. Natl. Acad. Sci. U. S. A. 77:1980;6473-6475
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6473-6475
    • Kotake, A.N.1    Funae, Y.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire M., Champeil P., Møller J.V. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508:2000;86-111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 22
    • 0029031273 scopus 로고
    • Interaction of cytochrome P4501A (CYP1A) genes from two teleost fish, toadfish (Opsanus tau) and scup (Stenotomis chrysops) and phylogenetic analysis of CYP1A genes
    • Morrison H.G., Oleksiat M.F., Cornell N.W., Sogin M.L., Stegeman J.J. Interaction of cytochrome P4501A (CYP1A) genes from two teleost fish, toadfish (Opsanus tau) and scup (Stenotomis chrysops) and phylogenetic analysis of CYP1A genes. Biochem. J. 308:1995;97-104
    • (1995) Biochem. J. , vol.308 , pp. 97-104
    • Morrison, H.G.1    Oleksiat, M.F.2    Cornell, N.W.3    Sogin, M.L.4    Stegeman, J.J.5
  • 23
    • 0345310056 scopus 로고    scopus 로고
    • Molecular cloning of CYP1A from the estuarine fish Fundulus heteroclitus and phylogenetic analysis if CYP1 genes: Update with new sequences
    • Morrison H.G., Weil E.J., Karchner S.I., Sogin M.L., Stegeman J.J. Molecular cloning of CYP1A from the estuarine fish Fundulus heteroclitus and phylogenetic analysis if CYP1 genes: update with new sequences. Comp. Biochem. Physiol. C121:1998;231-240
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 231-240
    • Morrison, H.G.1    Weil, E.J.2    Karchner, S.I.3    Sogin, M.L.4    Stegeman, J.J.5
  • 24
    • 0030585328 scopus 로고    scopus 로고
    • Preparation, purification, and spectrophotometric characterization of cytochrome P4501A2 conjugated with polyethyleneglycol monomethyl ether
    • Nakhgevany R., Bonsu O., Barber J., Mabrouk P.A., Ueng Y.F., Bell L.C., Guengerich F.P. Preparation, purification, and spectrophotometric characterization of cytochrome P4501A2 conjugated with polyethyleneglycol monomethyl ether. Biochem. Biophys. Res. Commun. 222:1996;406-409
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 406-409
    • Nakhgevany, R.1    Bonsu, O.2    Barber, J.3    Mabrouk, P.A.4    Ueng, Y.F.5    Bell, L.C.6    Guengerich, F.P.7
  • 25
    • 0033616138 scopus 로고    scopus 로고
    • Forty years of cytochrome P450
    • Omura T. Forty years of cytochrome P450. Biochem. Biophys Res. Commun. 266:1999;690-698
    • (1999) Biochem. Biophys Res. Commun. , vol.266 , pp. 690-698
    • Omura, T.1
  • 26
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its heme protein nature
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its heme protein nature. J. Biol. Chem. 239:1964;2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 27
    • 0017831699 scopus 로고
    • Direct fluorimetric methods for measuring mixed-function oxidase activity
    • Prough R.A., Burke M.D., Mayer B.T. Direct fluorimetric methods for measuring mixed-function oxidase activity. Methods Enzymol. 52:1978;374-377
    • (1978) Methods Enzymol. , vol.52 , pp. 374-377
    • Prough, R.A.1    Burke, M.D.2    Mayer, B.T.3
  • 28
  • 29
    • 0030594810 scopus 로고    scopus 로고
    • Chromatographic separation and behavior of microsomal cytochrome P450 and b5
    • Roos P.H. Chromatographic separation and behavior of microsomal cytochrome P450 and b5. J. Chromatogr. 684:1996;107-131
    • (1996) J. Chromatogr. , vol.684 , pp. 107-131
    • Roos, P.H.1
  • 30
    • 0025139447 scopus 로고
    • Purification and characterization of hepatic microsomal cytochrome P-450
    • Ryan D.E., Levin W. Purification and characterization of hepatic microsomal cytochrome P-450. Pharmacol. Ther. 45:1990;153-239
    • (1990) Pharmacol. Ther. , vol.45 , pp. 153-239
    • Ryan, D.E.1    Levin, W.2
  • 31
    • 0343118146 scopus 로고    scopus 로고
    • Separation of three P450 isoenzymes from liver microsomes of gilthead seabream treated with β-NF and partial purification of cytochrome P4501A1
    • Sen A., Arinç E. Separation of three P450 isoenzymes from liver microsomes of gilthead seabream treated with β-NF and partial purification of cytochrome P4501A1. Biochem. Mol. Biol. Int. 41:1997;131-141
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 131-141
    • Sen, A.1    Arinç, E.2
  • 32
    • 0031767369 scopus 로고    scopus 로고
    • Preparation of highly purified cytochrome P4501A1 from leaping mullet (Liza saliens) liver microsomes and its biocatalyst, molecular and immunochemical properties
    • Sen A., Arinç E. Preparation of highly purified cytochrome P4501A1 from leaping mullet (Liza saliens) liver microsomes and its biocatalyst, molecular and immunochemical properties. Comp. Biochem. Physiol. C121:1998;249-265
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 249-265
    • Sen, A.1    Arinç, E.2
  • 33
    • 0025869270 scopus 로고
    • Cytochrome P450 monoxygenase system in aquatic species: Carcinogen metabolism and biomarkers for carcinogen and pollutant exposure
    • Stegeman J.J., Lech J.J. Cytochrome P450 monoxygenase system in aquatic species: carcinogen metabolism and biomarkers for carcinogen and pollutant exposure. Environ. Health Perspect. 90:1991;101-109
    • (1991) Environ. Health Perspect. , vol.90 , pp. 101-109
    • Stegeman, J.J.1    Lech, J.J.2
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: Procedure and some application
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: procedure and some application. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0035811981 scopus 로고    scopus 로고
    • Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry
    • Villanueva J., Canals F., Querol E., Avilés F.X. Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry. Enzyme Microb. Technol. 29:2001;99-103
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 99-103
    • Villanueva, J.1    Canals, F.2    Querol, E.3    Avilés, F.X.4
  • 36
    • 0027949759 scopus 로고
    • Toxicological and ecological implication of biotransformation enzymes in tropical teleost Chaetodon capistratus
    • Vrolijk N.H., Targett N.M., Woodin B.R., Stegeman J.J. Toxicological and ecological implication of biotransformation enzymes in tropical teleost Chaetodon capistratus. Mar. Biol. 119:1994;151-158
    • (1994) Mar. Biol. , vol.119 , pp. 151-158
    • Vrolijk, N.H.1    Targett, N.M.2    Woodin, B.R.3    Stegeman, J.J.4
  • 37
    • 0029856855 scopus 로고    scopus 로고
    • Conformational changes of cytochrome P4501A2 induced by sodium chloride
    • Yun C.H., Songs M., Ahn T., Kim H. Conformational changes of cytochrome P4501A2 induced by sodium chloride. J. Biol. Chem. 271:1996;31312-31316
    • (1996) J. Biol. Chem. , vol.271 , pp. 31312-31316
    • Yun, C.H.1    Songs, M.2    Ahn, T.3    Kim, H.4
  • 38
    • 0030857439 scopus 로고    scopus 로고
    • Conformational changes of cytochrome P4501A2 induced by phospholipids and detergents
    • Yun C.H., Songs M., Kim H. Conformational changes of cytochrome P4501A2 induced by phospholipids and detergents. J. Biol. Chem. 272:1997;19725-19730
    • (1997) J. Biol. Chem. , vol.272 , pp. 19725-19730
    • Yun, C.H.1    Songs, M.2    Kim, H.3


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